Why are transmembrane domain made of hydrophobic amino acids?
Why are transmembrane domain made of hydrophobic amino acids?
Homework Answers
Transmembrane proteins are those which are embedded inside the membrane. They span both extracellular and intracellular side faces of the membrane.
The inside of the membrane is made up of hydrophobic fatty acids and is therefore hydrophobic in nature. This is called as hydrophobic core of the membrane.
For stable integration of transmembrane proteins into the hydrophobic core of the membrane, transmembrane proteins are rich in in hydraphobic amino acids which makes the transmembrane domain. The hydrophobic amino acids of transmembrane proteins can easily interact with hydrophobic fatty acid tails, thereby stabilizing the integration of transmembrane proteins into the membrane.
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It looks like a hydrophobic "pocket" in mdm-2 interacts with several hydrophobic amino acids in 2....
It looks like a hydrophobic "pocket" in mdm-2 interacts with several hydrophobic amino acids in 2. p53. What does hydrophobic mean and tell why the amino acids Phe, Leu and Trp are hydrophobic (what do you need to look at to tell if it is hydrophobic or not). Why do these hydrophobic molecules interact with each other?
Question 2 (1 point) Amino acids can be classified as A. Hydrophobic amino acids with nonpolar...
Question 2 (1 point) Amino acids can be classified as A. Hydrophobic amino acids with nonpolar R groups B. Polar amino acids with neutral R groups but the charge is not evenly distributed C. Positively charged amino acids with R groups that have positive charge at physiological pH. D. Negatively charged amino acids with R groups that have a negative charge at physiological pH. How would the amino acid alanine be classified? Think through your reasoning. L-Alanine H2N-CHC-OH CH3
For the tertiary structure of proteins in an aqueous/polar environment, hydrophobic amino acids are located on...
For the tertiary structure of proteins in an aqueous/polar environment, hydrophobic amino acids are located on the surface of the protein whereas non-polar amino acids are located in the interior. Let’s assume that the protein was normally in an environment with just the opposite composition, that is a non-polar, hydrophobic environment (for example liquid methane). What would the orientation of the polar and non-polar amino acids be? Explain.
For the tertiary structure of proteins in an aqueous/polar environment, hydrophobic amino acids are located on...
For the tertiary structure of proteins in an aqueous/polar environment, hydrophobic amino acids are located on the surface of the protein whereas non-polar amino acids are located in the interior. Let’s assume that the protein was normally in an environment with just the opposite composition, that is a non-polar, hydrophobic environment (for example liquid methane). What would the orientation of the polar and non-polar amino acids be? Explain.
1. Amino acids are considered to be either hydrophobic or hydrophilic as described by the relative...
1. Amino acids are considered to be either hydrophobic or hydrophilic as described by the relative polarity of their side chain. Consider a folded protein in an aqueous environment; where would the hydrophobic amino acids likely be found? -Tucked away in the middle of the folded protein -Randomly distributed throughout the protein -Exposed on the exterior surface of the folded protein 2. All proteins exhibit a primary, secondary, and tertiary structure, but not all proteins exhibit a quaternary structure. Describe...
You are in charge of designing hydrophobic α-amino acids. You are limited to using only saturated...
You are in charge of designing hydrophobic α-amino acids. You are limited to using only saturated alkyl R-groups of no more than 4 carbons. 4 of these α-amino acids are already found among the 20 common amino acids. Give their names and structural formulas. There are more than 4 other possible α-amino acids. Give their names and structural formulas. α-imino acids are not acceptable.
You are in charge of designing hydrophobic α-amino acids. You are limited to using only saturated...
You are in charge of designing hydrophobic α-amino acids. You are limited to using only saturated alkyl R-groups of no more than 4 carbons. 4 of these α-amino acids are already found among the 20 common amino acids? Give their names and structural formulas. (0.25 pt/per AA) There are more than 4 other possible α-amino acids. Give their names and structural formulas. α-amino acids are not acceptable. (0.25 pt/per AA)
Question 23 struct The interaction of the side chains on the amino acids, for example hydrophobic...
Question 23 struct The interaction of the side chains on the amino acids, for example hydrophobic attractions, is the Selected Answer: secondary Answers: secondary quaternary tertiary Aneu Question 24
Even though hydrophobic amino acids tend to be buried in the interior of a globular protein,...
Even though hydrophobic amino acids tend to be buried in the interior of a globular protein, polar neutral and polar charged amino acids are found in the interior of a globular protein as well. Recall Figure 4.26 of myoglobin. To see how this can happen, consider a model of a generic globular protein (below). The side chains of only seven of the amino acids are shown. 5. "DH" is a side chain that is a hydrogen bond donor "A" is...
true or false and why? The isoelectronic point of a protein is influenced by the hydrophobic...
true or false and why? The isoelectronic point of a protein is influenced by the hydrophobic amino acids
It looks like a hydrophobic "pocket" in mdm-2 interacts with several hydrophobic amino acids in 2. p53. What does hydrophobic mean and tell why the amino acids Phe, Leu and Trp are hydrophobic (what do you need to look at to tell if it is hydrophobic or not). Why do these hydrophobic molecules interact with each other?
Question 2 (1 point) Amino acids can be classified as A. Hydrophobic amino acids with nonpolar R groups B. Polar amino acids with neutral R groups but the charge is not evenly distributed C. Positively charged amino acids with R groups that have positive charge at physiological pH. D. Negatively charged amino acids with R groups that have a negative charge at physiological pH. How would the amino acid alanine be classified? Think through your reasoning. L-Alanine H2N-CHC-OH CH3
Question 23 struct The interaction of the side chains on the amino acids, for example hydrophobic attractions, is the Selected Answer: secondary Answers: secondary quaternary tertiary Aneu Question 24
Even though hydrophobic amino acids tend to be buried in the interior of a globular protein, polar neutral and polar charged amino acids are found in the interior of a globular protein as well. Recall Figure 4.26 of myoglobin. To see how this can happen, consider a model of a generic globular protein (below). The side chains of only seven of the amino acids are shown. 5. "DH" is a side chain that is a hydrogen bond donor "A" is...
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